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• W2889197028 abstract "AT exists as two isoforms differing in affinity for heparin (Thromb Res 27:23,1982; JBC 260:610,1985). The binding of human AT isoforms to commercial heparin, or purified unbleached heparin was studied. These heterogeneous, mixed-affinity (MA) heparins were coupled to agarose. When columns of these resins were eluted with NaCl gradients, after mixtures of the higher (ATvh) and lower (ATh) affinity isoforms of AT had been applied, ATvh always eluted after ATh. To determine the nature of this difference, low-affinity (LA) heparin was prepared by repeated passage of MA heparin over an ATh-ConA-Sepharose column. Neither AT isoform bound during passage over a LA-heparin agarose column equilibrated with 0.15 M NaCl. However, the ATvh was significantly retarded, while ATh eluted at about the same position as BSA. To demonstrate that ATh also interacts with a LA-site on heparin, a column containing MA heparin was loaded with ATh until the effluent concentration reached a steady state. Under the conditions, 21 mg of ATh was associated with the column in the steady state. Of this 10 mg eluted during a wash with 0.15 M NaCl, and 11 mg with 1.5 M NaCl elution. When the same experiment was performed using ATvh in place of ATh, approximately 25% more ATvh bound in both the steady state and to the washed column. To demonstrate that a secondary interaction is responsible for the separation of ATvh and ATh during heparin-agarose chromatography, the isoforms were applied together to MA-heparin columns in less than saturating amounts. When NaCl gradients were used to elute the columns in a reverse direction (bottom to top of column), ATh and ATvh co-eluted at relatively low salt concentrations. Thus, separation results during filtration of ATh and ATvh through the columns, after neutralization of the HA interaction. Finally, to determine if ATh and ATvh compete for the same binding sites on heparin, a MA-heparin column was loaded with a saturating amount of ATh. When ATvh was applied to this column, ATh was quantitatively displaced. It is concluded that (1) both AT isoforms bind LA sites on heparin (2) heparin contains many more LA sites than the HA ones; (3) ATvh binds more strongly to LA sites than ATh; and (4) LA binding may enhance activation of AT at the HA site by increasing the rate at which AT binds to this site." @default.
• W2889197028 created "2018-09-07" @default.
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• W2889197028 date "1987-01-01" @default.
• W2889197028 modified "2023-09-23" @default.
• W2889197028 title "EVIDENCE FOR SECONDARY SITES OF HEPARIN BINDING TO ANTITHROMBIN III (AT) ISOFORMS" @default.
• W2889197028 doi "https://doi.org/10.1055/s-0038-1643681" @default.
• W2889197028 hasPublicationYear "1987" @default.
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